RAP-1 is an Arabidopsis MYC-like R protein homologue, that binds to G-box sequence motifs

Plant Mol Biol. 1997 May;34(1):169-74. doi: 10.1023/a:1005898823105.


An Arabidopsis cDNA clone encoding a DNA-binding protein, RAP-1, was isolated by southwestern screening of an Escherichia coli cDNA expression library. The protein contains a bHLH DNA-binding domain and is homologous to R proteins, regulating anthocyanin biosynthesis. RAP-1 binds to the sequence CACNTG. It is encoded by a single gene, which is expressed to high levels in root and stem and to low levels in leaf and flower. No expression could be detected in siliques. Rap-1 does not correspond to one of the known loci involved in anthocyanin biosynthesis, since it is located at a different map position. In contrast to the maize R protein Lc, RAP-1 did not induce anthocyanin biosynthesis in pea cotyledons. Thus, RAP-1 is a novel member of the bHLH class of DNA-binding proteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / chemistry
  • Arabidopsis / genetics*
  • Arabidopsis / metabolism
  • Base Sequence
  • Binding Sites / genetics
  • Molecular Sequence Data
  • Plant Proteins / chemistry
  • Plant Proteins / genetics*
  • Plant Proteins / metabolism*
  • Proto-Oncogene Proteins c-myc / chemistry
  • Proto-Oncogene Proteins c-myc / genetics*
  • Proto-Oncogene Proteins c-myc / metabolism*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Trans-Activators / metabolism*


  • Plant Proteins
  • Proto-Oncogene Proteins c-myc
  • R-sc protein, Zea mays
  • Trans-Activators

Associated data

  • GENBANK/X99548